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Conserved domains on  [gi|15240468|ref|NP_200324|]
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co-factor for nitrate, reductase and xanthine dehydrogenase 5 [Arabidopsis thaliana]

Protein Classification

HesA/MoeB/ThiF family protein( domain architecture ID 10091539)

HesA/MoeB/ThiF family protein with a Rhodanese Homology Domain (RHOD), similar to adenylyltransferase and sulfurtransferases MOCS3 and UBA4 that play a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 71-299 9.93e-128

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


:

Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 369.50  E-value: 9.93e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 151 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 230
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240468 231 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 338-464 6.87e-57

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


:

Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 184.05  E-value: 6.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 338 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 417
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15240468 418 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 464
Cdd:cd01526  75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 122
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 71-299 9.93e-128

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 369.50  E-value: 9.93e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 151 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 230
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240468 231 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 65-311 3.44e-125

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 363.68  E-value: 3.44e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  65 SPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGH 144
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 145 PKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 224
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 225 NHNGGPCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRSS 304
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPGP--SCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                ....*..
gi 15240468 305 QCTVCGD 311
Cdd:COG0476 238 DCPVCGE 244
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-328 5.22e-116

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 345.46  E-value: 5.22e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   64 LSPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 143
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  144 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  224 YN----HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:PRK08762 268 FDagrqRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRL 347

                        250       260
                 ....*....|....*....|....*....
gi 15240468  300 RgRSSQCTVCGDNSSFNKQTfkdfDYEDF 328
Cdd:PRK08762 348 P-PDPHCPVCAPGRPFPGYI----DYAAF 371
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-308 3.96e-106

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 314.97  E-value: 3.96e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    72 YSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 151
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   152 AACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPC 231
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240468   232 YRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEP-LSERMLLFDALSARMRIVKIRGRSSQCTV 308
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnLAGRLLQFDALTMTFRELRLALKNPNCPV 238
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 71-272 2.52e-85

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 260.37  E-value: 2.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   151 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYN-HNGG 229
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDpGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15240468   230 PCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKL 272
Cdd:TIGR02356 161 PCLRCLFPDIADTGP--SCATAGVIGPVVGVIGSLQALEALKL 201
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 338-464 6.87e-57

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 184.05  E-value: 6.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 338 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 417
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15240468 418 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 464
Cdd:cd01526  75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 122
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 346-459 3.56e-22

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 90.80  E-value: 3.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 346 RISSKEFKEILQKkEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCRRG 425
Cdd:COG0607   5 EISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELP---KDK-------------PIVVYCASG 67

                        90       100       110
                ....*....|....*....|....*....|....
gi 15240468 426 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVNP 459
Cdd:COG0607  68 GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLP 101
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 358-459 2.54e-19

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 82.89  E-value: 2.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    358 KKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANteSCTNPSVFVVCRRGNDSQRAVQYLRE 437
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLG--LDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 15240468    438 SGFDSAKDIIGGLEAWAANVNP 459
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 357-454 3.94e-12

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 62.12  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   357 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANTEsctnpsVFVVCRRGNDSQRAVQYLR 436
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP------IVVYCNSGNRAAAAAALLK 74

                          90
                  ....*....|....*...
gi 15240468   437 ESGFDSAKDIIGGLEAWA 454
Cdd:pfam00581  75 ALGYKNVYVLDGGFEAWK 92
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
418-455 3.14e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.78  E-value: 3.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15240468  418 VFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 455
Cdd:PRK00162  61 VMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAWRR 98
 
Name Accession Description Interval E-value
ThiF_MoeB_HesA_family cd00757
ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis ...
 71-299 9.93e-128

ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1).


Pssm-ID: 238386 [Multi-domain]  Cd Length: 228  Bit Score: 369.50  E-value: 9.93e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:cd00757   1 RYSRQILLPEIGEEGQEKLKNARVLVVGAGGLGSPAAEYLAAAGVGKLGLVDDDVVELSNLQRQILHTEADVGQPKAEAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 151 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGP 230
Cdd:cd00757  81 AERLRAINPDVEIEAYNERLDAENAEELIAGYDLVLDCTDNFATRYLINDACVKLGKPLVSGAVLGFEGQVTVFIPGEGP 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240468 231 CYRCLFPTPPPTSaCQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:cd00757 161 CYRCLFPEPPPPG-VPSCAEAGVLGPLVGVIGSLQALEALKILLGIGEPLAGRLLLFDALSMSFRTLKL 228
ThiF COG0476
Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; ...
 65-311 3.44e-125

Molybdopterin or thiamine biosynthesis adenylyltransferase [Coenzyme transport and metabolism]; Molybdopterin or thiamine biosynthesis adenylyltransferase is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440244 [Multi-domain]  Cd Length: 244  Bit Score: 363.68  E-value: 3.44e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  65 SPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGH 144
Cdd:COG0476   1 TDEELERYSRQILLPEIGEEGQEKLKAARVLVVGAGGLGSPVALYLAAAGVGTLTLVDDDVVELSNLQRQILYTEADVGR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 145 PKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 224
Cdd:COG0476  81 PKVEAAAERLRALNPDVEVEAIPERLTEENALELLAGADLVLDCTDNFATRYLLNDACVKLGIPLVSGAVIGFEGQVTVF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 225 NHNGGPCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRSS 304
Cdd:COG0476 161 IPGDTPCYRCLFPEPPEPGP--SCAEAGVLGPLVGVIGSLQATEAIKLLTGIGEPLAGRLLLFDALTMEFRTIKLP-RDP 237


                ....*..
gi 15240468 305 QCTVCGD 311
Cdd:COG0476 238 DCPVCGE 244
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
64-328 5.22e-116

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 345.46  E-value: 5.22e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   64 LSPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 143
Cdd:PRK08762 108 LTDEQDERYSRHLRLPEVGEEGQRRLLEARVLLIGAGGLGSPAALYLAAAGVGTLGIVDHDVVDRSNLQRQILHTEDRVG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  144 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:PRK08762 188 QPKVDSAAQRLAALNPDVQVEAVQERVTSDNVEALLQDVDVVVDGADNFPTRYLLNDACVKLGKPLVYGAVFRFEGQVSV 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  224 YN----HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:PRK08762 268 FDagrqRGQAPCYRCLFPEPPPPELAPSCAEAGVLGVLPGVIGLLQATEAIKLLLGIGDPLTGRLLTFDALAMRFRELRL 347

                        250       260
                 ....*....|....*....|....*....
gi 15240468  300 RgRSSQCTVCGDNSSFNKQTfkdfDYEDF 328
Cdd:PRK08762 348 P-PDPHCPVCAPGRPFPGYI----DYAAF 371
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
64-464 4.42e-112

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 335.94  E-value: 4.42e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   64 LSPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 143
Cdd:PRK07411  11 LSKDEYERYSRHLILPEVGLEGQKRLKAASVLCIGTGGLGSPLLLYLAAAGIGRIGIVDFDVVDSSNLQRQVIHGTSWVG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  144 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:PRK07411  91 KPKIESAKNRILEINPYCQVDLYETRLSSENALDILAPYDVVVDGTDNFPTRYLVNDACVLLNKPNVYGSIFRFEGQATV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  224 YNHNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgRS 303
Cdd:PRK07411 171 FNYEGGPNYRDLYPEPPPPGMVPSCAEGGVLGILPGIIGVIQATETIKIILGAGNTLSGRLLLYNALDMKFRELKLR-PN 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  304 SQCTVCGdnssfnkqtfKDFDYEDFTQFP-LFAGPLNLLPAESRISSKEFKEILQK-KEQHVLLDVRPSHHYKIVSLPDS 381
Cdd:PRK07411 250 PERPVIE----------KLIDYEQFCGIPqAKAAEAAQKAEIPEMTVTELKALLDSgADDFVLIDVRNPNEYEIARIPGS 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  382 LNIPLANLETrlNELTSALKEKGNGHantesctnpSVFVVCRRGNDSQRAVQYLRESGFdSAKDIIGGLEAWAANVNPNF 461
Cdd:PRK07411 320 VLVPLPDIEN--GPGVEKVKELLNGH---------RLIAHCKMGGRSAKALGILKEAGI-EGTNVKGGITAWSREVDPSV 387


                 ...
gi 15240468  462 PTY 464
Cdd:PRK07411 388 PQY 390
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 55-464 2.96e-106

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 320.89  E-value: 2.96e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   55 LTAPELEhgLSPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQ 134
Cdd:PRK07878   8 LVEPAAE--LTRDEVARYSRHLIIPDVGVDGQKRLKNARVLVIGAGGLGSPTLLYLAAAGVGTLGIVEFDVVDESNLQRQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  135 IIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAA 214
Cdd:PRK07878  86 VIHGQSDVGRSKAQSARDSIVEINPLVNVRLHEFRLDPSNAVELFSQYDLILDGTDNFATRYLVNDAAVLAGKPYVWGSI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  215 LGMEGQLTVY---NHNG-GPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDAL 290
Cdd:PRK07878 166 YRFEGQASVFwedAPDGlGLNYRDLYPEPPPPGMVPSCAEGGVLGVLCASIGSIMGTEAIKLITGIGEPLLGRLMVYDAL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  291 SARMRIVKIRGRSSQCTVCgdnssfnkqtfKDFDYEDFTQfpLFAGPLNLLPAESRISSKEFKEILQKKEQHVLLDVRPS 370
Cdd:PRK07878 246 EMTYRTIKIRKDPSTPKIT-----------ELIDYEAFCG--VVSDEAQQAAAGSTITPRELKEWLDSGKKIALIDVREP 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  371 HHYKIVSLPDSLNIPLANLETrlneltsalkekgnGHANTESCTNPSVFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGL 450
Cdd:PRK07878 313 VEWDIVHIPGAQLIPKSEILS--------------GEALAKLPQDRTIVLYCKTGVRSAEALAALKKAGFSDAVHLQGGV 378

                        410
                 ....*....|....
gi 15240468  451 EAWAANVNPNFPTY 464
Cdd:PRK07878 379 VAWAKQVDPSLPMY 392
ThiF pfam00899
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ...
 72-308 3.96e-106

ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.


Pssm-ID: 459987 [Multi-domain]  Cd Length: 238  Bit Score: 314.97  E-value: 3.96e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    72 YSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 151
Cdd:pfam00899   1 YSRQLALPLIGEDGQEKLRNSRVLIVGAGGLGSEAAKYLARAGVGKITLVDFDTVELSNLNRQFLFREADIGKPKAEVAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   152 AACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPC 231
Cdd:pfam00899  81 ERLREINPDVEVEAYTERLTPENAEELIKSFDIVVDATDNFAARYLVNDACVKLGKPLIEAGVLGFKGQVTVVIPGKTPC 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240468   232 YRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEP-LSERMLLFDALSARMRIVKIRGRSSQCTV 308
Cdd:pfam00899 161 YRCLFPEDPPPKLVPSCTVAGVLGPTTAVVAGLQALEALKLLLGKGEPnLAGRLLQFDALTMTFRELRLALKNPNCPV 238
PRK05690 PRK05690
molybdopterin biosynthesis protein MoeB; Provisional
 64-306 3.49e-100

molybdopterin biosynthesis protein MoeB; Provisional


Pssm-ID: 180204 [Multi-domain]  Cd Length: 245  Bit Score: 299.84  E-value: 3.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   64 LSPDQIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 143
Cdd:PRK05690   5 LSDEEMLRYNRQIILRGFDFDGQEKLKAARVLVVGLGGLGCAASQYLAAAGVGTLTLVDFDTVSLSNLQRQVLHDDATIG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  144 HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:PRK05690  85 QPKVESARAALARINPHIAIETINARLDDDELAALIAGHDLVLDCTDNVATRNQLNRACFAAKKPLVSGAAIRMEGQVTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  224 YN-HNGGPCYRCLFPTPPPTSACqrCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRgR 302
Cdd:PRK05690 165 FTyQDDEPCYRCLSRLFGENALT--CVEAGVMAPLVGVIGSLQAMEAIKLLTGYGEPLSGRLLLYDAMTMQFREMKLK-R 241


                 ....
gi 15240468  303 SSQC 306
Cdd:PRK05690 242 DPGC 245
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 68-455 1.37e-90

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 279.45  E-value: 1.37e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   68 QIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKV 147
Cdd:PRK05597   5 DIARYRRQIMLGEIGQQGQQSLFDAKVAVIGAGGLGSPALLYLAGAGVGHITIIDDDTVDLSNLHRQVIHSTAGVGQPKA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  148 KSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHN 227
Cdd:PRK05597  85 ESAREAMLALNPDVKVTVSVRRLTWSNALDELRDADVILDGSDNFDTRHLASWAAARLGIPHVWASILGFDAQLSVFHAG 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  228 GGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKIRGRSSqct 307
Cdd:PRK05597 165 HGPIYEDLFPTPPPPGSVPSCSQAGVLGPVVGVVGSAMAMEALKLITGVGTPLIGKLGYYDSLDGTWEYIPVVGNPA--- 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  308 vcgdnssfnkqtfkdfdyedfTQFPLFAGPLNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLA 387
Cdd:PRK05597 242 ---------------------VLERVRGSTPVHGISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLS 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240468  388 NLEtrlneltsalkekgNGHANTESCTNPSVFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 455
Cdd:PRK05597 301 AIR--------------EGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWLD 354
adenyl_thiF TIGR02356
thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB ...
 71-272 2.52e-85

thiazole biosynthesis adenylyltransferase ThiF, E. coli subfamily; Members of the HesA/MoeB/ThiF family of proteins (pfam00899) include a number of members encoded in the midst of thiamine biosynthetic operons. This mix of known and putative ThiF proteins shows a deep split in phylogenetic trees, with the Escherichia. coli ThiF and the E. coli MoeB proteins seemingly more closely related than E. coli ThiF and Campylobacter (for example) ThiF. This model represents the more widely distributed clade of ThiF proteins such found in E. coli. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274094  Cd Length: 202  Bit Score: 260.37  E-value: 2.52e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:TIGR02356   1 RYARQLLLPDIGEEGQQRLLNSHVLIIGAGGLGSPAALYLAGAGVGTIVIVDDDHVDLSNLQRQILFTEEDVGRPKVEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   151 AAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYN-HNGG 229
Cdd:TIGR02356  81 AQRLRELNSDIQVTALKERVTAENLELLINNVDLVLDCTDNFATRYLINDACVALGTPLISAAVVGFGGQLMVFDpGGEG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 15240468   230 PCYRCLFPTPPPTSAcqRCSDSGVLGVVPGVIGCLQALETIKL 272
Cdd:TIGR02356 161 PCLRCLFPDIADTGP--SCATAGVIGPVVGVIGSLQALEALKL 201
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 338-464 6.87e-57

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 184.05  E-value: 6.87e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 338 LNLLPAESRISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSalkekgNGHANTESCTNPS 417
Cdd:cd01526   1 LKLLSPEERVSVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKS------LQELPLDNDKDSP 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15240468 418 VFVVCRRGNDSQRAVQYLRESGFDS-AKDIIGGLEAWAANVNPNFPTY 464
Cdd:cd01526  75 IYVVCRRGNDSQTAVRKLKELGLERfVRDIIGGLKAWADKVDPTFPLY 122
PRK05600 PRK05600
thiamine biosynthesis protein ThiF; Validated
 61-441 7.74e-57

thiamine biosynthesis protein ThiF; Validated


Pssm-ID: 235528 [Multi-domain]  Cd Length: 370  Bit Score: 192.40  E-value: 7.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   61 EHGLSPD------QIYRYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQ 134
Cdd:PRK05600   5 EHTLSPFmqlptsELRRTARQLALPGFGIEQQERLHNARVLVIGAGGLGCPAMQSLASAGVGTITLIDDDTVDVSNIHRQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  135 IIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAA 214
Cdd:PRK05600  85 ILFGASDVGRPKVEVAAERLKEIQPDIRVNALRERLTAENAVELLNGVDLVLDGSDSFATKFLVADAAEITGTPLVWGTV 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  215 LGMEGQLTVYN---HNGGPCYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALS 291
Cdd:PRK05600 165 LRFHGELAVFNsgpDHRGVGLRDLFPEQPSGDSIPDCATAGVLGATTAVIGALMATEAIKFLTGIGDVQPGTVLSYDALT 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  292 ARMRIVKIRGRSSQCTVCGDNSSFNKQTFKDFDYEDFTqfplfagplnlLPAESrisskefkeilqkkeqhVLLDVRPSH 371
Cdd:PRK05600 245 ATTRSFRVGADPARPLVTRLRPSYEAARTDTTSLIDAT-----------LNGSA-----------------TLLDVREPH 296

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  372 HYKIVSLPDSlnipLANLETRLNELTSalkEKGNGHANTESCTNpSVFVVCRRGNDSQRAVQYLRESGFD 441
Cdd:PRK05600 297 EVLLKDLPEG----GASLKLPLSAITD---DADILHALSPIDGD-NVVVYCASGIRSADFIEKYSHLGHE 358
PRK08328 PRK08328
hypothetical protein; Provisional
 64-299 1.73e-49

hypothetical protein; Provisional


Pssm-ID: 169382 [Multi-domain]  Cd Length: 231  Bit Score: 168.82  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   64 LSPDQIYRYSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIG 143
Cdd:PRK08328   2 LSERELERYDRQIMI--FGVEGQEKLKKAKVAVVGVGGLGSPVAYYLAAAGVGRILLIDEQTPELSNLNRQILHWEEDLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  144 -HPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLT 222
Cdd:PRK08328  80 kNPKPLSAKWKLERFNSDIKIETFVGRLSEENIDEVLKGVDVIVDCLDNFETRYLLDDYAHKKGIPLVHGAVEGTYGQVT 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240468  223 VYNHNGGPCYRCLFPTPPptsacQRCSDSGVLGVVPGVIGCLQALETIKLASLVGEPLSERMLLFDALSARMRIVKI 299
Cdd:PRK08328 160 TIVPGKTKRLREIFPKVK-----KKKGKFPILGATAGVIGSIQAMEVIKLITGYGEPLLNKLLIVDLANNVFEVVEL 231
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 71-380 3.41e-41

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 149.76  E-value: 3.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFI--GHPKVK 148
Cdd:PRK07688   4 RYSRQELFSPIGEEGQQKLREKHVLIIGAGALGTANAEMLVRAGVGKVTIVDRDYVEWSNLQRQQLYTESDVknNLPKAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  149 SAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 228
Cdd:PRK07688  84 AAKKRLEEINSDVRVEAIVQDVTAEELEELVTGVDLIIDATDNFETRFIVNDAAQKYGIPWIYGACVGSYGLSYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  229 GPCYRCLFPTPPptSACQRCSDSGVLGVVPGVIGCLQALETIKLasLVG--EPLSERMLLFD---ALSARMRIVKIrgRS 303
Cdd:PRK07688 164 TPCLRCLLQSIP--LGGATCDTAGIISPAVQIVASYQVTEALKL--LVGdyEALRDGLVSFDvwkNEYSCMNVQKL--KK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  304 SQCTVCGDnssfnKQTFKDFDYEDFTQFPLFAG-------PlnllPAESRISSKEFKEILQK-----KEQHVLLDVRpSH 371
Cdd:PRK07688 238 DNCPSCGE-----KALYPYLNYENTTKTAVLCGrntvqirP----PHKEEYDLEELAELLRDrgldvNVNPYLLSFS-LE 307


                 ....*....
gi 15240468  372 HYKIVSLPD 380
Cdd:PRK07688 308 EKRLVLFKD 316
PRK12475 PRK12475
thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional
 71-320 2.91e-38

thiamine/molybdopterin biosynthesis MoeB-like protein; Provisional


Pssm-ID: 183547 [Multi-domain]  Cd Length: 338  Bit Score: 142.18  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   71 RYSRQLLLPSFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTE--AFIGHPKVK 148
Cdd:PRK12475   4 RYSRQILFSGIGEEGQRKIREKHVLIVGAGALGAANAEALVRAGIGKLTIADRDYVEWSNLQRQQLYTEedAKQKKPKAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  149 SAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 228
Cdd:PRK12475  84 AAKEHLRKINSEVEIVPVVTDVTVEELEELVKEVDLIIDATDNFDTRLLINDLSQKYNIPWIYGGCVGSYGVTYTIIPGK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  229 GPCYRCLFPTPPPTSACqrCSDSGVLGVVPGVIGCLQALETIKLasLVG--EPLSERMLLFDALSARMRIVKI-RGRSSQ 305
Cdd:PRK12475 164 TPCLRCLMEHVPVGGAT--CDTAGIIQPAVQIVVAYQVTEALKI--LVEdfEALRETFLSFDIWNNQNMSIKVnKQKKDT 239

                        250
                 ....*....|....*
gi 15240468  306 CTVCGDNSSFNKQTF 320
Cdd:PRK12475 240 CPSCGLTRTYPSLTF 254
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 94-223 1.46e-33

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 123.53  E-value: 1.46e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  94 VLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTS 173
Cdd:cd01483   2 VLLVGLGGLGSEIALNLARSGVGKITLIDFDTVELSNLNRQFLARQADIGKPKAEVAARRLNELNPGVNVTAVPEGISED 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15240468 174 NALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:cd01483  82 NLDDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIDAGGLGLGGDIQV 131
YgdL_like cd00755
Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli ...
 84-214 6.46e-26

Family of activating enzymes (E1) of ubiquitin-like proteins related to the E.coli hypothetical protein ygdL. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238384 [Multi-domain]  Cd Length: 231  Bit Score: 105.38  E-value: 6.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  84 EGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKV 163
Cdd:cd00755   4 EGLEKLRNAHVAVVGLGGVGSWAAEALARSGVGKLTLIDFDVVCVSNLNRQIHALLSTVGKPKVEVMAERIRDINPECEV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15240468 164 DEYVEALRTSNALEILS-QYDIIVDATDNPPSRYMISDCCVLLGKPLVS--GAA 214
Cdd:cd00755  84 DAVEEFLTPDNSEDLLGgDPDFVVDAIDSIRAKVALIAYCRKRKIPVISsmGAG 137
PRK08644 PRK08644
sulfur carrier protein ThiS adenylyltransferase ThiF;
89-219 3.88e-25

sulfur carrier protein ThiS adenylyltransferase ThiF;


Pssm-ID: 236320 [Multi-domain]  Cd Length: 212  Bit Score: 102.63  E-value: 3.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   89 LLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQ---IIHteafIGHPKVKSAAAACRSINSTIKVDE 165
Cdd:PRK08644  26 LKKAKVGIAGAGGLGSNIAVALARSGVGNLKLVDFDVVEPSNLNRQqyfISQ----IGMPKVEALKENLLEINPFVEIEA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15240468  166 YVEALRTSNALEILSQYDIIVDATDNPPSRYMISDCCV-LLGKPLVsgAALGMEG 219
Cdd:PRK08644 102 HNEKIDEDNIEELFKDCDIVVEAFDNAETKAMLVETVLeHPGKKLV--AASGMAG 154
TcdA COG1179
tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and ...
 71-214 1.77e-24

tRNA A37 threonylcarbamoyladenosine dehydratase [Translation, ribosomal structure and biogenesis]; tRNA A37 threonylcarbamoyladenosine dehydratase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440792  Cd Length: 247  Bit Score: 101.70  E-value: 1.77e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  71 RYSR-QLLLPSfavEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKS 149
Cdd:COG1179   6 RFSRtERLYGE---EGLERLANAHVAVVGLGGVGSWAAEALARSGVGRLTLVDLDDVCESNINRQLHALDSTVGRPKVEV 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15240468 150 AAAACRSINSTIKVDEYVEALRTSNALEILSQ-YDIIVDATDN-PPSRYMISdCCVLLGKPLVS--GAA 214
Cdd:COG1179  83 MAERIRDINPDCEVTAIDEFVTPENADELLSEdYDYVIDAIDSvSAKAALIA-WCRRRGIPIISsmGAG 150
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 346-459 3.56e-22

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 90.80  E-value: 3.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 346 RISSKEFKEILQKkEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCRRG 425
Cdd:COG0607   5 EISPAELAELLES-EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELP---KDK-------------PIVVYCASG 67

                        90       100       110
                ....*....|....*....|....*....|....
gi 15240468 426 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVNP 459
Cdd:COG0607  68 GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLP 101
E1_ThiF_like cd01487
E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. ...
 93-219 3.80e-22

E1_ThiF_like. Member of superfamily of activating enzymes (E1) of the ubiquitin-like proteins. The common reaction mechanism catalyzed by E1-like enzymes begins with a nucleophilic attack of the C-terminal carboxylate of the ubiquitin-like substrate, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of the substrate. The exact function of this family is unknown.


Pssm-ID: 238764 [Multi-domain]  Cd Length: 174  Bit Score: 93.21  E-value: 3.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  93 SVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAfIGHPKVKSAAAACRSINSTIKVDEYVEALRT 172
Cdd:cd01487   1 KVGIAGAGGLGSNIAVLLARSGVGNLKLVDFDVVEPSNLNRQQYFLSQ-IGEPKVEALKENLREINPFVKIEAINIKIDE 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15240468 173 SNALEILSQYDIIVDATDNPPSRYMISDCCV-LLGKPLVSGAalGMEG 219
Cdd:cd01487  80 NNLEGLFGDCDIVVEAFDNAETKAMLAESLLgNKNKPVVCAS--GMAG 125
E1-2_like cd01484
Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present ...
 93-245 2.65e-21

Ubiquitin activating enzyme (E1), repeat 2-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the second repeat of Ub-E1.


Pssm-ID: 238761 [Multi-domain]  Cd Length: 234  Bit Score: 92.26  E-value: 2.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  93 SVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRT 172
Cdd:cd01484   1 KVLLVGAGGIGCELLKNLALMGFGQIHVIDMDTIDVSNLNRQFLFRPKDIGRPKSEVAAEAVNDRNPNCKVVPYQNKVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15240468 173 SN--ALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPCYRC-LFPTPPPTSAC 245
Cdd:cd01484  81 EQdfNDTFFEQFHIIVNALDNIIARRYVNGMLIFLIVPLIESGTEGFKGNAQVILPGMTECIECtLYPPQKNFPMC 156
Uba2_SUMO cd01489
Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating ...
 94-243 7.06e-20

Ubiquitin activating enzyme (E1) subunit UBA2. UBA2 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. UBA2 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238766 [Multi-domain]  Cd Length: 312  Bit Score: 90.13  E-value: 7.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  94 VLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALR-T 172
Cdd:cd01489   2 VLVVGAGGIGCELLKNLVLTGFGEIHIIDLDTIDLSNLNRQFLFRKKHVGKSKAQVAKEAVLSFNPNVKIVAYHANIKdP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240468 173 SNALEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNGGPCYRCLfPTPPPTS 243
Cdd:cd01489  82 DFNVEFFKQFDLVFNALDNLAARRHVNKMCLAADVPLIESGTTGFLGQVQVIKKGKTECYECQ-PKETPKT 151
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 358-459 2.54e-19

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 82.89  E-value: 2.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    358 KKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANteSCTNPSVFVVCRRGNDSQRAVQYLRE 437
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLG--LDKDKPVVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|..
gi 15240468    438 SGFDSAKDIIGGLEAWAANVNP 459
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGPP 100
PRK08223 PRK08223
hypothetical protein; Validated
 83-228 2.67e-17

hypothetical protein; Validated


Pssm-ID: 181302 [Multi-domain]  Cd Length: 287  Bit Score: 82.04  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   83 VEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIK 162
Cdd:PRK08223  19 PTEQQRLRNSRVAIAGLGGVGGIHLLTLARLGIGKFTIADFDVFELRNFNRQAGAMMSTLGRPKAEVLAEMVRDINPELE 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15240468  163 VDEYVEALRTSNALEILSQYDIIVDATD--NPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYNHNG 228
Cdd:PRK08223  99 IRAFPEGIGKENADAFLDGVDVYVDGLDffEFDARRLVFAACQQRGIPALTAAPLGMGTALLVFDPGG 166
Uba3_RUB cd01488
Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating ...
 93-241 6.55e-17

Ubiquitin activating enzyme (E1) subunit UBA3. UBA3 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins. consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. UBA3 contains both the nucleotide-binding motif involved in adenylation and the catalytic cysteine involved in the thioester intermediate and Ublp transfer to E2.


Pssm-ID: 238765 [Multi-domain]  Cd Length: 291  Bit Score: 80.86  E-value: 6.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  93 SVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRT 172
Cdd:cd01488   1 KILVIGAGGLGCELLKNLALSGFRNIHVIDMDTIDVSNLNRQFLFREKDIGKPKAEVAAKFVNDRVPGVNVTPHFGKIQD 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240468 173 SNaLEILSQYDIIVDATDN-PPSRYMISDCCVLLG-------KPLVSGAALGMEGQLTVYNHNGGPCYRCLFPTPPP 241
Cdd:cd01488  81 KD-EEFYRQFNIIICGLDSiEARRWINGTLVSLLLyedpesiIPLIDGGTEGFKGHARVILPGITACIECSLDLFPP 156
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 347-458 6.92e-16

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 73.20  E-value: 6.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 347 ISSKEFKEILQK-KEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKgnghantesctnpSVFVVCRRG 425
Cdd:cd01528   2 ISVAELAEWLADeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELDSDNPDK-------------DIVVLCHHG 68

                        90       100       110
                ....*....|....*....|....*....|...
gi 15240468 426 NDSQRAVQYLRESGFDSAKDIIGGLEAWAANVN 458
Cdd:cd01528  69 GRSMQVAQWLLRQGFENVYNLQGGIDAWSLEVD 101
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 351-454 1.24e-15

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 71.95  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 351 EFKEiLQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELtsalkekgNGHANTEsctnpsVFVVCRRGNDSQR 430
Cdd:cd00158   1 ELKE-LLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALL--------ELDKDKP------IVVYCRSGNRSAR 65

                        90       100
                ....*....|....*....|....
gi 15240468 431 AVQYLRESGFDSAKDIIGGLEAWA 454
Cdd:cd00158  66 AAKLLRKAGGTNVYNLEGGMLAWK 89
Ube1_repeat2 cd01490
Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present ...
 93-224 6.84e-14

Ubiquitin activating enzyme (E1), repeat 2. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the second repeat of Ub-E1.


Pssm-ID: 238767 [Multi-domain]  Cd Length: 435  Bit Score: 73.48  E-value: 6.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  93 SVLVIGAGGLG-----SPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYV 167
Cdd:cd01490   1 KVFLVGAGAIGcellkNFALMGVGTGESGEITVTDMDNIEKSNLNRQFLFRPHDVGKPKSEVAAAAVKAMNPDLKITALQ 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240468 168 EAL--RTSNAL--EILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVY 224
Cdd:cd01490  81 NRVgpETEHIFndEFWEKLDGVANALDNVDARMYVDRRCVYYRKPLLESGTLGTKGNTQVV 141
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 71-223 6.95e-14

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 74.15  E-value: 6.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468     71 RYSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGV-----GQLGIIDHDVVELNNMHRQIIHTEAFIGHP 145
Cdd:TIGR01408  401 RYDAQIAV--FGDTFQQKLQNLNIFLVGCGAIGCEMLKNFALMGVgtgkkGMITVTDPDLIEKSNLNRQFLFRPHHIGKP 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    146 KVKSAAAACRSINSTIKVDEYVEAL--RTSNAL--EILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQL 221
Cdd:TIGR01408  479 KSYTAADATLKINPQIKIDAHQNRVgpETETIFndEFYEKLDVVINALDNVEARRYVDSRCLAFLKPLLESGTLGTKGNT 558


                   ..
gi 15240468    222 TV 223
Cdd:TIGR01408  559 QV 560
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 357-454 3.94e-12

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 62.12  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   357 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTSALKEKGNGHANTEsctnpsVFVVCRRGNDSQRAVQYLR 436
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKP------IVVYCNSGNRAAAAAALLK 74

                          90
                  ....*....|....*...
gi 15240468   437 ESGFDSAKDIIGGLEAWA 454
Cdd:pfam00581  75 ALGYKNVYVLDGGFEAWK 92
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 346-455 1.79e-10

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 57.66  E-value: 1.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 346 RISSKEFKEILQKKEQHVLLDVRPSHHY--KIVSLPDSLNIPLANLETRLNELTsalKEKgnghantesctnpSVFVVCR 423
Cdd:cd01444   1 RISVDELAELLAAGEAPVLLDVRDPASYaaLPDHIPGAIHLDEDSLDDWLGDLD---RDR-------------PVVVYCY 64

                        90       100       110
                ....*....|....*....|....*....|..
gi 15240468 424 RGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 455
Cdd:cd01444  65 HGNSSAQLAQALREAGFTDVRSLAGGFEAWRR 96
PRK15116 PRK15116
sulfur acceptor protein CsdL; Provisional
 92-201 5.76e-10

sulfur acceptor protein CsdL; Provisional


Pssm-ID: 185071  Cd Length: 268  Bit Score: 59.82  E-value: 5.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   92 SSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKV---DEYVE 168
Cdd:PRK15116  31 AHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVtvvDDFIT 110

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15240468  169 AlrtSNALEILSQ-YDIIVDATDN-PPSRYMISDC 201
Cdd:PRK15116 111 P---DNVAEYMSAgFSYVIDAIDSvRPKAALIAYC 142
PRK14852 PRK14852
hypothetical protein; Provisional
 72-240 5.80e-10

hypothetical protein; Provisional


Pssm-ID: 184854 [Multi-domain]  Cd Length: 989  Bit Score: 61.64  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   72 YSRQLLLPSFAveGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 151
Cdd:PRK14852 315 FSRNLGLVDYA--GQRRLLRSRVAIAGLGGVGGIHLMTLARTGIGNFNLADFDAYSPVNLNRQYGASIASFGRGKLDVMT 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  152 AACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATD--NPPSRYMISDCCVLLGKPLVSGAALGMEGQLTVYnHNGG 229
Cdd:PRK14852 393 ERALSVNPFLDIRSFPEGVAAETIDAFLKDVDLLVDGIDffALDIRRRLFNRALELGIPVITAGPLGYSCALLVF-MPGG 471

                        170
                 ....*....|....*
gi 15240468  230 PCYRCLF----PTPP 240
Cdd:PRK14852 472 MNFDSYFgiddDTPP 486
PRK14851 PRK14851
hypothetical protein; Provisional
 52-228 5.93e-10

hypothetical protein; Provisional


Pssm-ID: 184853 [Multi-domain]  Cd Length: 679  Bit Score: 61.41  E-value: 5.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   52 DSYLTAPElEHGLSPDQIYR---YSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVEL 128
Cdd:PRK14851   4 DSHLETLQ-TLGISSAAEYReaaFSRNIGL--FTPGEQERLAEAKVAIPGMGGVGGVHLITMVRTGIGRFHIADFDQFEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  129 NNMHRQIIHTEAFIGHPKVKSAAAACRSINSTIKVDEYVEALRTSNALEILSQYDIIVDATD--NPPSRYMISDCCVLLG 206
Cdd:PRK14851  81 VNVNRQFGARVPSFGRPKLAVMKEQALSINPFLEITPFPAGINADNMDAFLDGVDVVLDGLDffQFEIRRTLFNMAREKG 160

                        170       180
                 ....*....|....*....|..
gi 15240468  207 KPLVSGAALGMEGQLTVYNHNG 228
Cdd:PRK14851 161 IPVITAGPLGYSSAMLVFTPQG 182
E1-1_like cd01485
Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present ...
 72-238 1.87e-09

Ubiquitin activating enzyme (E1), repeat 1-like. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. A set of novel molecules with a structural similarity to Ub, called Ub-like proteins (Ubls), have similar conjugation cascades. In contrast to ubiquitin-E1, which is a single-chain protein with a weakly conserved two-fold repeat, many of the Ubls-E1are a heterodimer where each subunit corresponds to one half of a single-chain E1. This CD represents the family homologous to the first repeat of Ub-E1.


Pssm-ID: 238762 [Multi-domain]  Cd Length: 198  Bit Score: 57.43  E-value: 1.87e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  72 YSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQ--IIHTEAFIGHPKVKS 149
Cdd:cd01485   2 YDRQIRL--WGDEAQNKLRSAKVLIIGAGALGAEIAKNLVLAGIDSITIVDHRLVSTEDLGSNffLDAEVSNSGMNRAAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 150 AAAACRSINSTIK---VDEYVEALrTSNALEILSQYDIIVdATDNPPSRYM-ISDCCVLLGKPLVSGAALGMEGQLtvyn 225
Cdd:cd01485  80 SYEFLQELNPNVKlsiVEEDSLSN-DSNIEEYLQKFTLVI-ATEENYERTAkVNDVCRKHHIPFISCATYGLIGYA---- 153

                       170
                ....*....|...
gi 15240468 226 hnggpcyRCLFPT 238
Cdd:cd01485 154 -------FFDFPI 159
APPBP1_RUB cd01493
Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric ...
 71-223 1.66e-08

Ubiquitin activating enzyme (E1) subunit APPBP1. APPBP1 is part of the heterodimeric activating enzyme (E1), specific for the Rub family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin(-like) by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by Rub family of ubiquitin-like proteins (Ublps) activates SCF ubiquitin ligases and is involved in cell cycle control, signaling and embryogenesis. ABPP1 contains part of the adenylation domain.


Pssm-ID: 238770 [Multi-domain]  Cd Length: 425  Bit Score: 56.54  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  71 RYSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVEL----NNMhrqIIHTEAfIGHPK 146
Cdd:cd01493   2 KYDRQLRL--WGEHGQAALESAHVCLLNATATGTEILKNLVLPGIGSFTIVDGSKVDEedlgNNF---FLDASS-LGKSR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 147 VKSAAAACRSINSTIK---VDEYVEALRTSNAlEILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSGAALGMEGQLTV 223
Cdd:cd01493  76 AEATCELLQELNPDVNgsaVEESPEALLDNDP-SFFSQFTVVIATNLPESTLLRLADVLWSANIPLLYVRSYGLYGYIRI 154
Aos1_SUMO cd01492
Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating ...
 72-219 1.91e-07

Ubiquitin activating enzyme (E1) subunit Aos1. Aos1 is part of the heterodimeric activating enzyme (E1), specific for the SUMO family of ubiquitin-like proteins (Ubls). E1 enzymes are part of a conjugation cascade to attach Ub or Ubls, covalently to substrate proteins consisting of activating (E1), conjugating (E2), and/or ligating (E3) enzymes. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and Ubls C-terminus. The E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Post-translational modification by SUMO family of ubiquitin-like proteins (Ublps) is involved in cell division, nuclear transport, the stress response and signal transduction. Aos1 contains part of the adenylation domain.


Pssm-ID: 238769 [Multi-domain]  Cd Length: 197  Bit Score: 51.14  E-value: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  72 YSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 151
Cdd:cd01492   4 YDRQIRL--WGLEAQKRLRSARILLIGLKGLGAEIAKNLVLSGIGSLTILDDRTVTEEDLGAQFLIPAEDLGQNRAEASL 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15240468 152 AACRSINSTIKVDEYVEALRTSNAlEILSQYDIIVdATDnpPSRYM---ISDCCVLLGKPLVSGAALGMEG 219
Cdd:cd01492  82 ERLRALNPRVKVSVDTDDISEKPE-EFFSQFDVVV-ATE--LSRAElvkINELCRKLGVKFYATGVHGLFG 148
Apg7 cd01486
Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and ...
 93-259 2.30e-07

Apg7 is an E1-like protein, that activates two different ubiquitin-like proteins, Apg12 and Apg8, and assigns them to specific E2 enzymes, Apg10 and Apg3, respectively. This leads to the covalent conjugation of Apg8 with phosphatidylethanolamine, an important step in autophagy. Autophagy is a dynamic membrane phenomenon for bulk protein degradation in the lysosome/vacuole.


Pssm-ID: 238763 [Multi-domain]  Cd Length: 307  Bit Score: 52.38  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  93 SVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHT--EAFIGHPKVKSAAAACRSINSTIKVD------ 164
Cdd:cd01486   1 KCLLLGAGTLGCNVARNLLGWGVRHITFVDSGKVSYSNPVRQSLFTfeDCKGGKPKAEAAAERLKEIFPSIDATgivlsi 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 165 ----------EYVEALRTSNALEIL-SQYDIIVDATDNPPSRYMISDCCVLLGKpLVSGAALGMEGQLTVYNHNGGPCYR 233
Cdd:cd01486  81 pmpghpisesEVPSTLKDVKRLEELiKDHDVIFLLTDSRESRWLPTLLSAAKNK-LVINAALGFDSYLVMRHGAGPQSQS 159

                       170       180       190
                ....*....|....*....|....*....|.
gi 15240468 234 CLFP-----TPPPTSACQRCSDSgvlgVVPG 259
Cdd:cd01486 160 GSGDsssdsIPGSRLGCYFCNDV----VAPG 186
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 357-453 9.97e-07

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 46.49  E-value: 9.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 357 QKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNELTsalKEKGnghantesctnpsVFVVCRRGNDSQRAVQYLR 436
Cdd:cd01524   9 YRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELP---KDKE-------------IIVYCAVGLRGYIAARILT 72

                        90
                ....*....|....*..
gi 15240468 437 ESGFDsAKDIIGGLEAW 453
Cdd:cd01524  73 QNGFK-VKNLDGGYKTY 88
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
418-455 3.14e-06

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 45.78  E-value: 3.14e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15240468  418 VFVVCRRGNDSQRAVQYLRESGFDSAKDIIGGLEAWAA 455
Cdd:PRK00162  61 VMVMCYHGNSSQGAAQYLLQQGFDVVYSIDGGFEAWRR 98
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
363-459 3.19e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.24  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  363 VLLDVRPSHHYKIVSLPDSLNIPLANLETRLNEltsALKEKGNghantesctnpSVFVVCRRGNDSQRAVQYLRESGFDS 442
Cdd:PRK08762  19 VLIDVREAHERASGQAEGALRIPRGFLELRIET---HLPDRDR-----------EIVLICASGTRSAHAAATLRELGYTR 84

                         90
                 ....*....|....*..
gi 15240468  443 AKDIIGGLEAWAANVNP 459
Cdd:PRK08762  85 VASVAGGFSAWKDAGLP 101
Ube1_repeat1 cd01491
Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present ...
 72-207 4.32e-06

Ubiquitin activating enzyme (E1), repeat 1. E1, a highly conserved small protein present universally in eukaryotic cells, is part of cascade to attach ubiquitin (Ub) covalently to substrate proteins. This cascade consists of activating (E1), conjugating (E2), and/or ligating (E3) enzymes and then targets them for degradation by the 26S proteasome. E1 activates ubiquitin by C-terminal adenylation, and subsequently forms a highly reactive thioester bond between its catalytic cysteine and ubiquitin's C-terminus. E1 also associates with E2 and promotes ubiquitin transfer to the E2's catalytic cysteine. Ubiquitin-E1 is a single-chain protein with a weakly conserved two-fold repeat. This CD represents the first repeat of Ub-E1.


Pssm-ID: 238768 [Multi-domain]  Cd Length: 286  Bit Score: 48.42  E-value: 4.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468  72 YSRQL-LLPSFAVegqSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSA 150
Cdd:cd01491   2 YSRQLyVLGHEAM---KKLQKSNVLISGLGGLGVEIAKNLILAGVKSVTLHDTKPCSWSDLSSQFYLREEDIGKNRAEAS 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 151 AAACRSINSTIKVDEYVEALRTsnalEILSQYDIIV-------------DATDNPPSRYMISDCCVLLGK 207
Cdd:cd01491  79 QARLAELNPYVPVTVSTGPLTT----DELLKFQVVVltdasledqlkinEFCHSPGIKFISADTRGLFGS 144
E1_like_apg7 TIGR01381
E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic ...
 77-311 2.47e-05

E1-like protein-activating enzyme Gsa7p/Apg7p; This model represents a family of eukaryotic proteins found in animals, plants, and yeasts, including Apg7p (YHR171W) from Saccharomyces cerevisiae and GSA7 from Pichia pastoris. Members are about 650 to 700 residues in length and include a central domain of about 150 residues shared with the ThiF/MoeB/HesA family of proteins. A low level of similarity to ubiquitin-activating enzyme E1 is described in a paper on peroxisome autophagy mediated by GSA7, and is the basis of the name ubiquitin activating enzyme E1-like protein. Members of the family appear to be involved in protein lipidation events analogous to ubiquitination and required for membrane fusion events during autophagy.


Pssm-ID: 273590 [Multi-domain]  Cd Length: 664  Bit Score: 46.86  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468    77 LLPSFAVEGQSNLlksSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIH--TEAFI-GHPKVKSAAAA 153
Cdd:TIGR01381 327 LHPDLQLERYSQL---KVLLLGAGTLGCNVARCLIGWGVRHITFVDNGKVSYSNPVRQSLSnfEDCLLgGRGKAETAQKA 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   154 CRSINSTIKVDEYV----------------EALRTSNAL-EILSQYDIIVDATDNPPSRYMISDCCVLLGKPLVSgAALG 216
Cdd:TIGR01381 404 LKRIFPSIQATGHRltvpmpghpidekdvpELEKDIARLeQLIKDHDVVFLLLDSREARWLPTVLCSRHKKIAIS-AALG 482

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468   217 MEGQLtVYNHNGGP-------------------CYRCLFPTPPPTSACQRCSDSGVLGVVPGVIGCLQALETIKLASLVG 277
Cdd:TIGR01381 483 FDSYV-VMRHGIGRsesvsdvsssdsvpysrlgCYFCNDVTAPGDSTTDRTLDQQCTVTRPGTAMIASGLAVELLVSVLQ 561

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 15240468   278 EPLSERM--------LLFDALSARMR--------IVKIRGRSSQCTVCGD 311
Cdd:TIGR01381 562 HPLPSKTpashddntTVLGALPHQIRgflgrfqqILLSVKRFDQCVACSD 611
Ube1 TIGR01408
ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino ...
 72-202 3.51e-05

ubiquitin-activating enzyme E1; This model represents the full length, over a thousand amino acids, of a multicopy family of eukaryotic proteins, many of which are designated ubiquitin-activating enzyme E1. Members have two copies of the ThiF family domain (pfam00899), a repeat found in ubiquitin-activating proteins (pfam02134), and other regions.


Pssm-ID: 273603 [Multi-domain]  Cd Length: 1006  Bit Score: 46.42  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468     72 YSRQLLLpsFAVEGQSNLLKSSVLVIGAGGLGSPALLYLAACGVGQLGIIDHDVVELNNMHRQIIHTEAFIGHPKVKSAA 151
Cdd:TIGR01408    7 YSRQLYV--LGDEAMQKMAKSNVLISGMGGLGLEIAKNLVLAGVKSVTLHDTEKCQAWDLSSNFFLSEDDVGRNRAEAVV 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 15240468    152 AACRSINSTIKVDEYVEALRTsnalEILSQYDIIVDATDNPPSRYMISDCC 202
Cdd:TIGR01408   85 KKLAELNPYVHVSSSSVPFNE----EFLDKFQCVVLTEMSLPLQKEINDFC 131
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 363-455 9.95e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 41.49  E-value: 9.95e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 363 VLLDVRPSHHYKIVSLPDSLNIPLANLETRLNeLTSALKEKGNGHANTESCTNpsVFVVCRRGNDSQRAVQYLRESGFDS 442
Cdd:cd01519  17 VLIDVREPEELKTGKIPGAINIPLSSLPDALA-LSEEEFEKKYGFPKPSKDKE--LIFYCKAGVRSKAAAELARSLGYEN 93

                        90
                ....*....|...
gi 15240468 443 AKDIIGGLEAWAA 455
Cdd:cd01519  94 VGNYPGSWLDWAA 106
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 346-396 2.69e-03

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 37.44  E-value: 2.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15240468 346 RISSKEFKEILQKKEQHVLLDVRPSHHYKIVSLPDSLNIPLANLETRLNEL 396
Cdd:cd01533  11 SVSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGEL 61
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 347-451 4.77e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 36.92  E-value: 4.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240468 347 ISSKEFKEILQKKEQHVLLDVRP-SHHYKIVSLPDSLNIPLANLET--RLNELTSALKEKGNGHAntesctnpSVFVVCR 423
Cdd:cd01522   1 LTPAEAWALLQADPQAVLVDVRTeAEWKFVGGVPDAVHVAWQVYPDmeINPNFLAELEEKVGKDR--------PVLLLCR 72

                        90       100
                ....*....|....*....|....*...
gi 15240468 424 RGNDSQRAVQYLRESGFDSAKDIIGGLE 451
Cdd:cd01522  73 SGNRSIAAAEAAAQAGFTNVYNVLEGFE 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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